The Journal of Cell Biology, Vol 89, 695-699, Copyright © 1981 by The Rockefeller University Press

ARTICLES

Presence and indirect immunofluorescent localization of calmodulin in Paramecium tetraurelia

NJ Maihle, JR Dedman, AR Means, JG Chafouleas and BH Satir

In this paper we demonstrate the presence and localization of calmodulin, a calcium-dependent regulatory protein, in the ciliated protozoan Paramecium tetraurelia. Calmodulin is demonstrated by several criteria: (a) the ability of whole cell Paramecium extracts to stimulate mammalian phosphodiesterase activity, (b) the presence of an acidic, thermostable, 17,000-dalton polypeptide whose mobility shifts in SDS polyacrylamide gel electrophoresis in the presence of Ca2+, and (c) the affinity of antibodies against mammalian calmodulin for a Paramecium component as demonstrated by both indirect immunofluorescent localization and radioimmunoassay. Indirect immunofluorescence studies reveal that Paramecium calmodulin is distributed in three distinct regions of the cell, i.e., (a) large, spherical cytoplasmic organelles representing perhaps the food vacuoles or other vacuolar inclusions of the cell, (b) along the entire length of oral and somatic cilia, and (c) along a linear punctate pattern corresponding to the kinetics (basal bodies) of the cell.
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This article has been cited by other articles:

• Walczak, C., Nelson, D. (1993). In vitro phosphorylation of ciliary dyneins by protein kinases from Paramecium. J. Cell Sci. 106: 1369-1376 [Abstract]  

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